Information on EC 1.3.3.6 - acyl-CoA oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.3.3.6
-
RECOMMENDED NAME
GeneOntology No.
acyl-CoA oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
acts on CoA derivatives of fatty acids with chain length from 8 to 18
-
-
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA; stereochemistry of the reaction
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
inducible by growth on di-(2-ethylhexyl)phthalate
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
genetic regulation
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
mechanism, substrate binding site, and active site structure
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
structural analysis of enzyme complexed with 3-ketoacyl-CoA substrate analogues
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
reduction
-
-
-
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
10-cis-heptadecenoyl-CoA degradation (yeast)
-
10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast)
-
6-gingerol analog biosynthesis
-
9-cis, 11-trans-octadecadienoyl-CoA degradation (isomerase-dependent, yeast)
-
alpha-Linolenic acid metabolism
-
Biosynthesis of unsaturated fatty acids
-
fatty acid beta-oxidation (peroxisome, yeast)
-
fatty acid beta-oxidation II (peroxisome)
-
fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent)
-
fatty acid beta-oxidation VI (peroxisome)
-
Fatty acid degradation
-
jasmonic acid biosynthesis
-
Metabolic pathways
-
methyl ketone biosynthesis
-
oleate beta-oxidation (isomerase-dependent, yeast)
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:oxygen 2-oxidoreductase
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
-
ACO
Q33DR1
-
ACO
Arthrobacter sp. 02.04.2001
Q33DR1
-
-
ACO
Arthrobacter ureafaciens NBRC 12140
Q33DR0
-
-
ACO
Beauveria bassiana GHA
-
-
-
ACO
Candida sp.
-
-
ACO
Sporidiobolus ruineniae CBS5001
-
-
-
ACO-A1
Q33DR0
recombinant enzyme
ACO-A1
Arthrobacter ureafaciens NBRC 12140
Q33DR0
recombinant enzyme
-
ACOX
Cucurbita sp.
-
-
ACOX
-
-
ACOX
-
-
ACOX
-
-
ACOX1
-
-
ACOX1
Q15067
-
ACOX1
-
-
ACOX1-3I
Q4QRE2
-
ACOX1a
-
isoform
ACOX1b
-
isoform
ACOX13II
-
-
ACX
Arabidopsis thaliana Col-0
-
-
-
ACX1
O65202
preference for medium to long chain acyl-CoAs and jasmonic acid-CoA
ACX1
Q5VRH3
-
ACX1.2
Q9ZQP2
also known as ACX5, its substrate preference overlaps considerably with ACX1 for long chain acyl-CoA substrates and influences jasmonic acid synthesis
ACX2
O65201
favours very long chain acyl-CoAs
ACX2
-
-
ACX3
Q9LLH9
favours medium chain acyl-CoA oxidation
ACX3
Q69XR7
-
ACX4
Q96329
has preference for short chain acyl-CoAs
acyl coenzyme A oxidase
-
-
-
-
Acyl-CoA oxidase
-
-
-
-
Acyl-CoA oxidase
Q8HYL8
-
Acyl-CoA oxidase
-
-
Acyl-CoA oxidase
-
-
Acyl-CoA oxidase
Yarrowia lipolytica W29
-
-
-
acyl-CoA oxidase 1
-
-
acyl-CoA oxidase 1
-
-
acyl-CoA oxidase 1a
-
isoform
acyl-CoA oxidase 1b
-
isoform
acyl-CoA oxidase 2
-
-
acyl-CoA oxidase 4
-
-
acyl-CoA oxidase 4
Arabidopsis thaliana Col-0
-
-
-
acyl-CoA oxidase I
-
-
acyl-CoA oxidase-II
-
-
acyl-CoA-oxidase
Q15067
-
acyl-coenzyme A oxidase
Q33DR1
-
acyl-coenzyme A oxidase
Arthrobacter sp. 02.04.2001
Q33DR1
-
-
acyl-coenzyme A oxidase
Q33DR0
-
acyl-coenzyme A oxidase
Arthrobacter ureafaciens NBRC 12140
Q33DR0
-
-
acyl-coenzyme A oxidase
Candida sp.
-
-
acyl-coenzyme A oxidase 1
-, Q4QRE2
-
acyl-coenzyme A oxidase 1
-
-
acyl-coenzyme A: oxygen oxidoreductase
Q33DR0
-
acyl-coenzyme A: oxygen oxidoreductase
Arthrobacter ureafaciens NBRC 12140
Q33DR0
-
-
AOX
-
-
-
-
AOX
Yarrowia lipolytica W29
-
-
-
Aox3p
Yarrowia lipolytica W29
-
-
-
Aoxp
Yarrowia lipolytica W29
-
-
-
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
-
fatty acyl-coenzyme A oxidase
-
-
-
-
long chain acyl-CoA oxidase
-
-
long chain fatty acyl coenzyme A oxidase
-
-
long chain fatty acyl-CoA oxidase
-
-
long-chain-specific acyl-CoA oxidase 1
-
-
MCAD Y375K
-
Y375K mutant of medium-chain acyl-CoA dehydrogenase that exhibits acyl-CoA oxidase activity
MCOX
-
-
oxidase, acyl-coenzyme A
-
-
-
-
palmitoyl-CoA oxidase
-
-
peroxisomal acyl-coenzyme A oxidase
-
-
Peroxisomal fatty acyl-CoA oxidase
-
-
-
-
Pristanoyl-CoA oxidase
-
-
-
-
SCOX
-
-
SCOX
-
-
short chain-specific acyl-CoA oxidase
Q96329
-
short-chain acyl-CoA oxidase
-
-
straight chain acyl-CoA oxidase
Q15067
-
straight-chain acyl-coenzyme A oxidase
-
-
THCA-CoA oxidase
-
-
-
-
THCCox
-
-
-
-
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
61116-22-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
O65201, Q9LLH9
SwissProt
Manually annotated by BRENDA team
ACX3
Q9LLH9
SwissProt
Manually annotated by BRENDA team
Col-0 accession
-
-
Manually annotated by BRENDA team
isoforms AtACX1, AtACX2, and AtACX3
-
-
Manually annotated by BRENDA team
isoforms AtACX1, AtACX2, AtACX3, and AtSACX
Uniprot
Manually annotated by BRENDA team
six ACX genes, acx1-acx6. ACX6 is not expressed
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
six ACX genes, acx1-acx6. ACX6 is not expressed
-
-
Manually annotated by BRENDA team
strain 2-4-1
SwissProt
Manually annotated by BRENDA team
Arthrobacter sp. 02.04.2001
strain 2-4-1
SwissProt
Manually annotated by BRENDA team
strain NBRC 12140
Q33DR0
SwissProt
Manually annotated by BRENDA team
Arthrobacter ureafaciens NBRC 12140
strain NBRC 12140
Q33DR0
SwissProt
Manually annotated by BRENDA team
strain GHA
-
-
Manually annotated by BRENDA team
Beauveria bassiana GHA
strain GHA
-
-
Manually annotated by BRENDA team
Candida sp.
-
-
-
Manually annotated by BRENDA team
pK 233, inducible by growth on alkanes
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
Cucurbita sp.
pumpkin
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene aoxA
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
ACOX1a and ACOX1b isoforms are encoded by a single gene
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
no activity in Sporidiobolus pararoseus
strain CBS484
-
-
Manually annotated by BRENDA team
no activity in Sporidiobolus pararoseus CBS484
strain CBS484
-
-
Manually annotated by BRENDA team
-
Q5VRH3, Q69XR7
SwissProt
Manually annotated by BRENDA team
3 forms: 1. inducible fatty acyl-CoA oxidase, 2. noninducible fatty acyl-CoA oxidase, 3. noninducible trihydroxycoprostanoyl-CoA oxidase
-
-
Manually annotated by BRENDA team
inducible by growth on di-(2-ethylhexyl)phthalate
-
-
Manually annotated by BRENDA team
two isoforms: ACO-I, ACO-II
-
-
Manually annotated by BRENDA team
oleate-inducible
-
-
Manually annotated by BRENDA team
strain CBS5001
-
-
Manually annotated by BRENDA team
Sporidiobolus ruineniae CBS5001
strain CBS5001
-
-
Manually annotated by BRENDA team
from Lophius americanus
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
i.e. Yarrowia lipolytica; isoform AOX3
-
-
Manually annotated by BRENDA team
six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
-
-
Manually annotated by BRENDA team
strain W29 (ATCC 20460)
-
-
Manually annotated by BRENDA team
Yarrowia lipolytica W29
six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
-
-
Manually annotated by BRENDA team
Yarrowia lipolytica W29
strain W29 (ATCC 20460)
-
-
Manually annotated by BRENDA team
medium-chain specific isoform, MCOX, and short-chain specific isoform, SCOX
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
deletion of gene aoxA leads to reduced growth on long chain fatty acids, but growth is not abolished by this mutation
malfunction
-
the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type. Reducing ACX4 expression in several Arabidopsis backgrounds shows a split response, suggesting that the ACX4 gene and/or protein functions differently in Arabidopsis accessions, phenotypes, detailed overview. ACX2 levels are increased in acx1acx3acx4Col compared to Col-0 wild-type samples
malfunction
Arabidopsis thaliana Col-0
-
the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type. Reducing ACX4 expression in several Arabidopsis backgrounds shows a split response, suggesting that the ACX4 gene and/or protein functions differently in Arabidopsis accessions, phenotypes, detailed overview. ACX2 levels are increased in acx1acx3acx4Col compared to Col-0 wild-type samples
-
metabolism
-
SCOX is the first enzyme of the peroxisomal beta-oxidation system and is involved in the oxidation of various fatty acids including very-long-chain fatty acids, long-chain dicarboxylic acids and polyunsaturated fatty acids, but not branched-chain fatty acids such as pristanic acid and the C27-bile acid intermediates
metabolism
-
ACOX1 is the first and rate-limiting enzyme of the peroxisomal beta-oxidation pathway
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation pathway
metabolism
-
the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
physiological function
-
involved in fatty acid oxidation, essential energy generation
physiological function
-
ACOX1b controls the spontaneous hepatic peroxisome proliferation
metabolism
Yarrowia lipolytica W29
-
the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
-
additional information
-
adult peroxisomal acyl-coenzyme A oxidase deficiency, formerly also called pseudoneonatal adrenoleucodystrophy, is a disorder of peroxisomal fatty acid oxidation with a severe presentation with cerebellar and brainstem atrophy, phenotype, overview. Accumulation of very-long-chain fatty acids is the only diagnostic marker for SCOX deficiency
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,16-hexadecadioyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
16-hydroxy-palmitoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
2-oxoheptadecyldethio-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4,8,12-trimethyl-tridecanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-nonanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
6-phenyl-6-phenyl-hexanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
O65201, Q9LLH9
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
3'-phosphate on the ribose ring and the structure of the adenine moiety are essential for substrate recognition, specificity is relatively low with respect to the structure of the pantric acid moiety
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
isoform ACO-I prefers short-chain acyl-CoA substrates, isoform ACO-II prefers long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
isoform SCOX prefers C4-C8 substrates, isoform MCOX prefers C10-C14 substrates
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
specificity: C4-C20 acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
enzyme acts selectively on fatty acyl-CoA with 16 or 18 carbon atoms, cis-9-unsaturated esters with a C16 or C18 acyl moiety being converted with higher rate than saturated or polyunsaturated fatty acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
chain-length specificity changes with acyl-CoA concentration used
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
highly specific for short-chain fatty acids
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
most active towards C12-C18 acyl-CoA, C20 and C22 acyl-CoA also oxidized, C4 and C6 acyl-CoA hardly oxidized
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
both isoforms ACX1.1 and 1.2 show similar broad substrate specificities
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
preference for long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Cucurbita sp.
-
preference for long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
AtACX1 is medium-chain specific, AtACX2 is medium- to long-chain specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C4-C18 monocarboxylic acid-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
C6-C16 dicarboxylic-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
medium-chain-length specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
long- and short-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtACX3 is medium-chain-specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
AtACX3 is medium-chain-specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtACX1 is medium- to long-chain specific, AtSACXis strictly short-chain specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
AtACX1 is medium- to long-chain specific, AtSACXis strictly short-chain specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
preference for C12-C18 acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Cucurbita sp.
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in lignin degradative system
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
beta-oxidation of dicarboxylic acid-CoAs in rat liver is carried out exclusively in peroxisomes
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
significance in metabolism of alkanes of Candida tropicalis
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
key enzyme of beta-oxidation. A basal level of long chain ACX is always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes. The enzyme plays a role not only during oil reserve mobilization, but also in plant growth and metabolism
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Yarrowia lipolytica W29
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Sporidiobolus ruineniae CBS5001
-
-
-
-
?
acyl-CoA + O2
trans-2-enoyl-CoA + H2O2
show the reaction diagram
-
assay at 25C
-
-
ir
arachidoyl-CoA + O2
2-trans-eicosenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
behenoyl-CoA + O2
2-trans-docosenoyl-CoA + H2O2
show the reaction diagram
Beauveria bassiana, Beauveria bassiana GHA
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
-
not
-
-
-
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
-
not
-
-
-
cis-3-decenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
cis-3-hexenoyl-CoA + O2
?
show the reaction diagram
-
best substrate for the isomerase activity of the enzyme
-
-
?
cis-3-octenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
dec-4-trans-enoyl-CoA + O2
2-trans-4-trans-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
-
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
O74935, -
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
dicarboxylic acid-CoAs with 6-16 carbon atoms + O2
?
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
O74935, -
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtACX3 and AtACX1 show preference for
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
preferred substrate of ACX3
-
-
?
eicosapentaenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
furylpropionyl-CoA + O2
furylacryloyl-CoA + H2O2
show the reaction diagram
-
also oxidizes aromatic/heterocyclic ring-substituted chromogenic substrates
-
?
hexadecanedioyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
hexadecanedioyl-CoA + O2
?
show the reaction diagram
O74935, -
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
-
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
-
recombinant enzyme
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
P0CZ23
AtSACX shows preference for
-
-
?
indole-3-butyric acid-CoA + O2
?
show the reaction diagram
-
-
-
-
?
jasmonic acid-CoA + O2
?
show the reaction diagram
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
preferred substrate of ACX1
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
-
low activity
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
P07872
binding mode of C12-fatty acid suggests that the active site does not close upon substrate binding, but remains spacious during the entire catalytic process, the oxygen accessibility in the oxidative half-reaction thereby being maintained
-
-
?
leuko-dichlorofluorescein + O2
?
show the reaction diagram
-
-
-
-
?
lignoceroyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
lignoceroyl-CoA + O2
?
show the reaction diagram
Beauveria bassiana, Beauveria bassiana GHA
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
O74935, -
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-, Q33DR0
highest activity
-
-
ir
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
AtACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-, Q33DR0
maximum activity
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
preferred substrate of ACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
Arthrobacter ureafaciens NBRC 12140
Q33DR0
highest activity
-
-
ir
nonanoyl-CoA + O2
trans-2-nonenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octadecanoyl-CoA + O2
?
show the reaction diagram
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
preferred substrate of ACX2
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
-
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-, Q8HYL8
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-, Q33DR0
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-, Q33DR0
-
-
-
ir
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Beauveria bassiana GHA
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
Arthrobacter ureafaciens NBRC 12140
Q33DR0
-
-
-
?, ir
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
isozyme ACOX1b shows higher activity than isozyme ACOX1a
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
AtACX2
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
Beauveria bassiana GHA
-
-
-
-
?
trans-3-decenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trans-3-hexenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trans-3-octenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trihydroxycoprostanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
structural and functional comparison of isoforms with each other and enzymes from other species, regulatory aspects
-
-
-
additional information
?
-
-
Aox2p expression regulates the size of cellular triacylglycerol pools and the size and number of intracellular lipid bodies in which these gatty acids accumulate
-
-
-
additional information
?
-
-
Eucalyptus terpenes elevate hepatic AOX expression in possum
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
-, Q8HYL8
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
O74935, -
no activity with hexadecanoyl-CoA and 3-methylheptadecanoyl-CoA
-
-
-
additional information
?
-
-, Q33DR0
high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6
-
-
-
additional information
?
-
-, Q33DR0
exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
additional information
?
-
Arabidopsis thaliana, Arabidopsis thaliana Col-0
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
additional information
?
-
Arthrobacter ureafaciens NBRC 12140
Q33DR0
high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6, exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
P0CZ23
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
Cucurbita sp.
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
involved in lignin degradative system
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
beta-oxidation of dicarboxylic acid-CoAs in rat liver is carried out exclusively in peroxisomes
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
significance in metabolism of alkanes of Candida tropicalis
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
-
key enzyme of beta-oxidation. A basal level of long chain ACX is always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes. The enzyme plays a role not only during oil reserve mobilization, but also in plant growth and metabolism
-
-
?
additional information
?
-
-
Aox2p expression regulates the size of cellular triacylglycerol pools and the size and number of intracellular lipid bodies in which these gatty acids accumulate
-
-
-
additional information
?
-
-
Eucalyptus terpenes elevate hepatic AOX expression in possum
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
-, Q8HYL8
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
Arabidopsis thaliana, Arabidopsis thaliana Col-0
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
flavoprotein
FAD
-
1.22 mol per mol of enzyme; flavoprotein; prosthetic group
FAD
-
flavoprotein; flavoprotein with noncovalently bound FAD
FAD
-
flavoprotein with noncovalently bound FAD
FAD
-
8 mol FAD per mol of enzyme, 1 mol FAD per mol of subunit; flavoprotein
FAD
-
tightly bound FAD, 4 mol per mol of enzyme octamer
FAD
-
both subunits are involved in FAD-binding
FAD
-
flavoprotein with noncovalently bound FAD
FAD
-
required for the isomerase activity of the enzyme
FAD
-, Q33DR0
flavoenzyme with 1 mol FAD per subunit; one molecule of non-covalently bound FAD per subunit as a prosthetic group
FAD
Candida sp.
-
-
FAD
-, Q4QRE2
;
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-bromopalmitic acid
-
-
2-Bromopalmitoyl-CoA
-
-
2-tetradecylglycidic acid
-
-
3,4-pentadienoyl-CoA
-
rapid, irreversible
3-ketoacyl-CoA substrate analogues
-
complex formation with anionic forms of 3-ketoacyl-CoA
3-ketohexadecanoyl-CoA
-
-
3-octynoyl-CoA
-
irreversible
5,5'-dithiobis(2-nitro-benzoic acid)
-
inactivates by modification of sulfhydryl groups and loss of FAD
acetyl-CoA
-
competitive inhibition
antimycin A
-
with addition of rotenone
C16-C18 fatty acyl-CoA
-
at fairly low concentrations
Detergents
-
inactiviation via dissociation of subunits
Detergents
-
no inhibition with Triton-X 100
FMN
-
uncompetitive inhibition
indole-3-butyric acid
-
inhibits root elongation
N-ethylmaleimide
Q33DR1
shows less than 10% activity in the presence of 10 mM at 37C for 4 h
N-ethylmaleimide
-, Q33DR0
ACO retains more than 60% of the initial activity in the presence of 10 mM N-ethylmaleimide, at 37C for 4 h; purified enzyme retains more than 60% activity in the presence of 10 mM at 37C for 4 h, while other commercially available ACOs show only less than 10% activities after the same treatment
N-ethylmaleimide
Candida sp.
-
shows less than 10% activity in the presence of 10 mM at 37 C for 4 h
oct-2-en-4-ynoyl-CoA
-
irreversible inactivation, pH dependent, higher under basic condition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
slight inhibition
Phenol
-
high concentration, magnitude of inhibition depends on the nature of the acyl-CoA substrate
Phenylmethylsulfonylfluoride
-
slight inhibition
Mercuric acetate
-
-
additional information
-
glutathione protects against inhibition with sulfhydryl reagents
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
enhances acyl-CoA oxidation, avoids H2O2 consumption by endogenous catalase
alpha-linolenic acid-rich perilla oil
-
stimulates
-
Bovine serum albumin
-
slightly increases ACO activity, maximum value of ACO acitvity at 0.036 mM
-
casein
O74935, -
stimulates
di-(2-ethylhexyl)phthalate
-
-
fish oil
-
markedly increases enzyme activity
-
growth hormone
-
increases the mRNA of acyl CoA oxidase, directly induces the expression of AOX in adipocytes through STAT5A binding to the -1841 to -1825 site within the AOX promoter
-
jasmonate
-, Q5VRH3, Q69XR7
upregulates expression of ACX1, starts 4 h after treatment and remains elevated until 24 h
leptin
-
3fold increased activity at 100 ng/ml acute treatment
-
n-Alkane
-
increases ACO activity progressively with palmitoyl-CoA by 23%, with stearoyl-CoA by 42%, with behenoyl-CoA by 47% and with lignoceroyl-CoA by 75%
-
perilla oil
-
elevates AOX activity in a 4-day fedding, the effect is gradually decreased in a 4-week feeding
-
Peroxidase
-
stimulates, maximum value of ACO acitvity at 0.24 mg
-
Phenol
-
low concentration, magnitude of activation depends on the nature of the acyl-CoA substrate
prolactin
-
increases the mRNA of acyl CoA oxidase
-
Propionate
-
increase in propionate concentration lead to increase of enzyme amount
tetracosane
-
stimulates, highest activity with lignoceroyl-CoA as substrate
Triton X-100
-
stimulates, maximum value of ACO acitvity at 0.08%
MnCl2
-
slightly activating
additional information
-, Q5VRH3, Q69XR7
no upregulation by jasmonate; no upregulation by jasmonate
-
additional information
-
AOX stimulation is highly associated with the content of long chain n-3 polyunsaturated fatty acids
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0335
-
arachidoyl-CoA
-
-
0.032
-
Butyryl-CoA
-
-
0.1319
-
Butyryl-CoA
-
-
0.044
-
cis-3-decenoyl-CoA
-
mutant E421D
0.054
-
cis-3-decenoyl-CoA
-
wild-type
0.063
-
cis-3-hexenoyl-CoA
-
wild-type
0.076
-
cis-3-hexenoyl-CoA
-
mutant E421D
0.054
-
cis-3-Octenoyl-CoA
-
mutant E421D
0.057
-
cis-3-Octenoyl-CoA
-
wild-type
0.0093
-
Dec-4-cis-enoyl-CoA
-
-
0.002
-
Decanoyl-CoA
-
recombinant enzyme
0.0072
-
Decanoyl-CoA
O74935, -
30C
0.02
-
Decanoyl-CoA
-
-
0.024
-
Decanoyl-CoA
-
-
0.002
-
Dodecanoyl-CoA
-
MCOX
0.0157
-
Dodecanoyl-CoA
P0CZ23
isozyme AtACX3
0.0189
-
Dodecanoyl-CoA
P0CZ23
isozyme AtACX1
0.025
-
Dodecanoyl-CoA
-
pH 7.0-9.5
0.071
-
Dodecanoyl-CoA
-
pH 6.2
0.1
-
Dodecanoyl-CoA
O74935, -
30C
0.00633
-
Hexadecanedioyl-CoA
O74935, -
30C
0.006
-
Hexanoyl-CoA
-
isozyme SCOX
0.02
-
Hexanoyl-CoA
P0CZ23
isozyme AtSACX
0.03
-
Hexanoyl-CoA
-
in 50 mM phosphate buffer, pH 7.4, at 30C
0.067
-
Hexanoyl-CoA
-
recombinant enzyme
0.092
-
Hexanoyl-CoA
-
-
0.013
-
Lauroyl-CoA
-
-
0.024
-
Lauroyl-CoA
-
-
0.027
-
Lauroyl-CoA
-
liver enzyme
0.0025
-
lignoceroyl-CoA
-
-
0.0073
-
linoleoyl-CoA
-
-
0.0053
-
myristoyl-CoA
-
isozyme AtACX1
0.011
-
myristoyl-CoA
-
-
0.011
-
myristoyl-CoA
-
-
0.0116
-
myristoyl-CoA
-
-
0.029
-
myristoyl-CoA
-
-
0.042
-
Octanoyl-CoA
-
-
0.0443
-
Octanoyl-CoA
-
pH 7.4, 30C, wild-type enzyme
0.0546
-
Octanoyl-CoA
-
pH 7.4, 30C, mutant enzyme E421D
0.058
-
Octanoyl-CoA
-
-
0.061
-
Octanoyl-CoA
-
-
0.087
-
Octanoyl-CoA
-
liver enzyme
0.011
-
oleoyl-CoA
-
-
0.046
-
oleoyl-CoA
-
-
0.00000002
-
palmitoyl-CoA
-, Q33DR0
-
0.00181
-
palmitoyl-CoA
-
kidney enzyme
0.007
-
palmitoyl-CoA
-
liver enzyme
0.01
-
palmitoyl-CoA
-
recombinant enzyme from Spodoptera frugiperda cells
0.0116
-
palmitoyl-CoA
-
-
0.02
-
palmitoyl-CoA
-
-
0.028
-
palmitoyl-CoA
-, Q8HYL8
AOX1
0.038
-
palmitoyl-CoA
-, Q8HYL8
AOX2
0.073
-
palmitoyl-CoA
-
isoform ACOX1a
0.09
-
palmitoyl-CoA
-
isoform ACOX1b
0.0044
-
stearoyl-CoA
-
isozyme AtACX2
0.0096
-
stearoyl-CoA
-
-
0.023
-
stearoyl-CoA
-
-
0.034
-
stearoyl-CoA
-
-
0.018
-
tetradecanoyl-CoA
O74935, -
30C
0.056
-
trans-3-decenoyl-CoA
-
wild-type
0.064
-
trans-3-decenoyl-CoA
-
mutant E421D
0.063
-
trans-3-hexenoyl-CoA
-
wild-type
0.083
-
trans-3-hexenoyl-CoA
-
mutant E421D
0.059
-
trans-3-octenoyl-CoA
-
wild-type
0.066
-
trans-3-octenoyl-CoA
-
mutant E421D
0.019
-
linoleoyl-CoA
-
-
additional information
-
additional information
-
overview: Km of several monocarboxylic and dicarboxylic acyl-CoA as substrates
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.225
-
Butyryl-CoA
-
-
0.04
-
cis-3-decenoyl-CoA
-
mutant E421D
0.06167
-
cis-3-decenoyl-CoA
-
wild-type
0.165
-
cis-3-hexenoyl-CoA
-
mutant E421D
0.35
-
cis-3-hexenoyl-CoA
-
wild-type
0.053
-
cis-3-Octenoyl-CoA
-
mutant E421D
0.075
-
cis-3-Octenoyl-CoA
-
wild-type
1.53
-
Decanoyl-CoA
-
recombinant enzyme
0.089
-
Hexanoyl-CoA
-
in 50 mM phosphate buffer, pH 7.4, at 30C
0.203
-
Hexanoyl-CoA
-
-
0.07
-
Octanoyl-CoA
-
-
2.18
-
Octanoyl-CoA
-
pH 7.4, 30C, mutant enzyme E421D
3.47
-
Octanoyl-CoA
-
pH 7.4, 30C, wild-type enzyme
78
-
palmitoyl-CoA
-, Q33DR0
-
0.0053
-
trans-3-decenoyl-CoA
-
mutant E421D
0.01567
-
trans-3-decenoyl-CoA
-
wild-type
0.0283
-
trans-3-hexenoyl-CoA
-
mutant E421D
0.05
-
trans-3-hexenoyl-CoA
-
wild-type
0.012
-
trans-3-octenoyl-CoA
-
mutant E421D
0.045
-
trans-3-octenoyl-CoA
-
wild-type
8.59
-
Hexanoyl-CoA
-
recombinant enzyme
additional information
-
additional information
-
pH-dependency of turnover number
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00047
-
3-ketohexadecanoyl-CoA
-
-
0.3
-
acetyl-CoA
-
-
0.03
-
CoA
-
low concentration
0.32
-
CoA
-
high concentration
0.045
-
oct-2-en-4-ynoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000016
-
-
activity in one peroxisomal acyl-coenzyme A oxidase deficiency patient, pH not specified in the publication, temperature not specified in the publication
0.0006
-
-
liver homogenate
0.00502
-
-
glucose-grown cultures with stearoyl-CoA as substrate
0.00571
-
-
glucose-grown cultures with behenoyl-CoA as substrate
0.00613
-
-
glucose-grown cultures with palmitoyl-CoA as substrate
0.00615
-
-
glucose-grown cultures with lignoceroyl-CoA as substrate
0.00714
-
-
alkane-grown cultures with stearoyl-CoA as substrate
0.00758
-
-
alkane-grown cultures with palmitoyl-CoA as substrate
0.008
4
-
alkane-grown cultures with behenoyl-CoA as substrate
0.0108
-
-
alkane-grown cultures with lignoceroyl-CoA as substrate
0.375
-
-
purified isozyme SCOX
1.7
-
-, Q33DR0
crude enzyme; crude extract, at 37C
1.95
-
-
recombinant enzyme, purified
2.04
-
-
purified enzyme
2.12
-
-
purified enzyme
5.3
-
-
highly purified isozyme MCOX
19.7
-
O74935, -
-
27
-
-
purified enzyme
27.2
-
-
purified enzyme
58
-
-
purified enzyme
60.9
-
-, Q33DR0
purified enzyme; purified recombinant enzyme, at 37C
77.14
-
-
purified enzyme
additional information
-
-
overview: specific activity of enzyme from several sources with several substrates
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
isoform ACOX1a exhibits only 50% specific activity toward palmitoyl-CoA as compared to ACOX1b; specific activities in units/mg for isoform ACOX1a: 0.186 for eicosapentaenoyl-CoA, 0.237 for 4-methyl-nonanoyl-CoA, 0.15 for 16-hydroxy-palmitoyl-CoA, 0.336 for 4,8,12-trimethyl-tridecanoyl-CoA, 0.372 for 1,16-hexadecadioyl-CoA, 0.699 for 6-phenyl-6-phenyl-hexanoyl-CoA, 0.076 for palmitoyl-CoA, specific activities in units/mg for isoform ACOX1b: 0.226 for eicosapentaenoyl-CoA, 0.278 for 4-methyl-nonanoyl-CoA, 0.298 for 16-hydroxy-palmitoyl-CoA, 0.423 for 4,8,12-trimethyl-tridecanoyl-CoA, 0.504 for 1,16-hexadecadioyl-CoA, 0.573 for 6-phenyl-6-phenyl-hexanoyl-CoA, 0.166 for palmitoyl-CoA
additional information
-
-
no activity in a second peroxisomal acyl-coenzyme A oxidase deficiency patient
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
recombinant enzyme
7.5
8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1b
7.5
-
-, Q33DR0
-
8.3
8.5
-
-
8.3
8.6
-
isozyme SCOX
8.5
-
-
optimal palmitoyl-CoA oxidase activity for ACOX1a
8.6
-
-
isozyme MCOX
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
10
-
pH 7: about 30% of activity maximum, pH 10: about 5% of activity maximum, inactive below pH 6.5
7.2
9.3
-
both isoforms
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
28
38
-
recombinant enzyme
37
-
-
assay at
37.5
-
-
the ACOX1b isoform has a maximum specific activity around 37.5C
40
-
-
the maximum specific activity for ACOX1a is obtained at 40C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
55
-
recombinant enzyme, at 5C, 21% activity, at 55C, 78% activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q4QRE2
;
Manually annotated by BRENDA team
-, Q4QRE2
discreetly expressed, lower levels of transcript variant ACOX13II, the ACOX13II transcript variant is expressed seven times more in brain than the ACOX13I variant; discreetly expressed, lower levels of transcript variant ACOX1-3I, the ACOX1-3I transcript variant is expressed seven times less in brain than the ACOX1-3II variant
Manually annotated by BRENDA team
-
developing, germinating
Manually annotated by BRENDA team
-, Q4QRE2
acox1 transcripts diffusely distributed in early-stage embryonic cells; acox1 transcripts diffusely distributed in early-stage embryonic cells
Manually annotated by BRENDA team
-, Q4QRE2
widely present at later stages, high levels of transcript variant ACOX13II in the anterior intestine, significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding; widely present at later stages, high levels of transcript variants ACOX1-3I in the anterior intestine, significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
Manually annotated by BRENDA team
-
significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
Manually annotated by BRENDA team
-, Q4QRE2
;
Manually annotated by BRENDA team
-, Q5VRH3, Q69XR7
-
Manually annotated by BRENDA team
-, Q4QRE2
widely present at later stages, high levels of transcript variant ACOX1-3I; widely present at later stages, high levels of transcript variant ACOX13II
Manually annotated by BRENDA team
-
before anthesis
Manually annotated by BRENDA team
-, Q5VRH3, Q69XR7
-
Manually annotated by BRENDA team
Cucurbita sp.
-
-
Manually annotated by BRENDA team
-, Q5VRH3, Q69XR7
ACX1 barely detectable; ACX3 expression less prominent compared to ACX2; predominant expression of ACX2
Manually annotated by BRENDA team
-, Q5VRH3, Q69XR7
-
Manually annotated by BRENDA team
-
low content
Manually annotated by BRENDA team
additional information
-
always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes
Manually annotated by BRENDA team
additional information
-
SK32 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Cucurbita sp.
-
-
Manually annotated by BRENDA team
-
existence of two independent, Pex5p-mediated import pathways into peroxisomes in yeast: 1. a classical peroxisomal targeting signal 1 pathway and a novel, non-PTS1 pathway for Pox1p
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0, Sporidiobolus ruineniae CBS5001
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-
SDS-PAGE
60000
-
-
isoform SCOX, gel filtration
62000
-
-
isoform MCOX, gel filtration
72000
-
-
Western blot analysis
76400
-
Q33DR1
predicted
76500
-
-, Q33DR0
predicted from amino acid sequence
81000
-
-
isoform ACOX1a and ACOX1b, SDS-PAGE
100000
-
-
gel filtration
136000
-
-
gel filtration
139000
-
-
sedimentation equilibrium method
139000
-
-
noninducible trihydroxycoprostanoyl-CoA oxidase
140000
-
-
native AtACX1 and AtACX2, and recombinant AtACX1, gel filtration
145000
-
-
inducible fatty acyl-CoA oxidase, gel filtration
150000
-
-
gel filtration
150000
-
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
-
160000
-
-, Q33DR0
native-PAGE
180000
-
-, Q33DR0
SDS-PAGE, recombinant enzyme
188000
-
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
ACX4
190000
-
-, Q33DR0
gel filtration; gel filtration, recombinant enzyme
427000
-
-
noninducible fatty acyl-CoA oxidase, gel filtration
552000
-
-
ultracentrifugation
600000
-
-
sedimentation equilibrium
660000
-
-
recombinant AtACX2, aggregation in E. coli, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
? * 52000 + ? * 22500, liver, SDS-PAGE, inducible fatty acyl-CoA oxidase
?
Cucurbita sp.
-
? * 73000, SDS-PAGE and sequence determination
?
-
? * 51000 + ? * 21000, recombinant enzyme, SDS-PAGE
?
-
? * 15000, isoform SCOX, labile multimeric structure, SDS-PAGE
?
-, Q33DR0
x * 76500, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
Arthrobacter ureafaciens NBRC 12140
-
x * 76500, SDS-PAGE
-
dimer
-
2 * 71000, liver, SDS-PAGE, noninducible fatty acyl-CoA oxidase
dimer
-
2 * 72000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 74300, AtACX1 and AtACX2, sequence determination
hexamer
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
homodimer
-, Q33DR0
2 * 75000, SDS-PAGE; 2 * 95000, gel filtration
homodimer
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
2 * 75000; 2 * 75000; 2 * 75000
homodimer
Arthrobacter ureafaciens NBRC 12140
-
2 * 75000, SDS-PAGE; 2 * 95000, gel filtration
-
homotetramer
O65201, O65202, Q96329, Q9LLH9, Q9ZQP2
4 * 47000, ACX4
monomer
-
1 * 62000, isoform MCOX, SDS-PAGE
octamer
-
8 * 75000, SDS-PAGE
octamer
-
8 * 72100, SDS-PAGE
tetramer
-
2 * 45000 + 2 * 22000, SDS-PAGE
tetramer
-
crystallographic studies
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by the hanging drop vapor diffusion technique, ACX4-acetoacetyl-CoA crystals to 2.7 A resolution, of His-tagged ACX4 to 3.9 A resolution
-
hanging-drop vapor-diffusion method, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 85.6 A, b = 117.0 A, c = 1313.3 A
-
hanging-drop vapour-diffusion method, the crystals diffract to 2.0 A using synchrotron radiation, have unit-cell parameters a = 85.2, b = 118.0, c = 131.0 A, alpha = beta = gamma = 90 and show P2(1)2(1)2(1) symmetry
-
at 5C from a 30% saturated ammonium sulfate solution, yellow rod-shaped crystals
-
cocrystallization of ACO-II with lauroyl-CoA by the hanging-drop vapor-diffusion method under oil, to 2.07 A resolution
P07872
native ACO-II, hanging-drop vapor-diffusion method with 3% (w/v) polyethylene glycol 20000 as precipitant in 20 mM potassium phosphate, pH 7.4; X-ray structure analysis
-
to 2.74 A resolution by vapor diffusion hanging-drop method, unusual packing arrangement of the tomato AXC1 enzyme as compared to other ACX enzymes, three monomers of ACX1 are present in the asymmetric unit
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9
-
35C, 60 min
6.5
7.5
-, Q33DR0
at 37C
7
9
-
stable for 120 min
additional information
-
-, Q33DR0
between 6.57.5 at 37C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
40
-
stable for 120 min
37.5
70
-
the ACOX1b isoform retains 57% of its specific activity at 50C and is more resistant to heat denaturation than ACOX1a since it conserves 30% of its specific activity after treatment at 50C, the isoform shows 70% specific activity at 37.5C
50
-
-
10 min
50
-
-
the specific activity of isoform ACOX1a drops to zero at 50C
60
-
-
30 min, with butyryl-CoA and FAD, 50% loss of activity; 30 min, with butyryl-CoA, without FAD, 85% loss of activity
65
-
-
10 min, complete inactivation
additional information
-
-
FAD enhances thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dialysis, 4C, 24 h, 80% loss of activity
-
stabilization with benzoate necessary for purification of the holoenzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, potassium phosphate buffer, pH 7.0
-, Q33DR0
37C, 0.2 M potassium phosphate (pH 7.5) containing 0.1 M FAD, 4 h, less than 10% loss of activity
-, Q33DR0
-20C, 25% glycerol, 8 months
-
-20C, pH 7.4, 2 months
-
4C, pH 7.4, 2 months, 20% loss of activity
-
frozen, 10% sucrose, several weeks
-
-20C, for at least 1 month
-
-80C, wild-type enzyme and mutant enzymes E421D, E421A, E421Q and E421G are stable for 3 months
-
4C, His-tagged enzyme is stable for 1 week
-
-30C, 35% glycerol (v/v), at least 1 month
-
-30C, in presence of 35% v/v glycerol, stable for at least 1 year
O74935, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by gel filtration and anion exchange chromatography
-
recombinant from Escherichia coli
P0CZ23
by gel filtration; Q-Sepharose column chromatography and CM-Sepharose column chromatography
-, Q33DR0
partially
Cucurbita sp.
-
Ni-NTA column chromatography
-
partially
-
recombinant His-tagged from Spodoptera frugiperda cells
-
ACO-i and ACO-II, recombinant from Escherichia coli
-
holo- and apoenzyme
-
native and recombinant ACO-II from Escherichia coli
-
nickel metal-affinity resin column chromatography
-
to homogeneity
-
recombinant from Escherichia coli, His-tagged
-
both isoforms
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli BL 21
-
expression in Escherichia coli of His-tagged proteins: AtSACX, AtACX1, and AtACX3, sequence analysis also with AtACX2
P0CZ23
expression of AtACX1 and AtACX2 in Escherichia coli; plant anti-sense constructs, investigation of substrate specificities and regulation
-
into the pET24 vector and transformed into Escherichia coli BL21(DE3)
-
into vector pUTE300, expression in Escherichia coli JM109
Q33DR1
expressed in Escherichia coli JM109 cells; into vector pUTE300, expression in Escherichia coli JM109
-, Q33DR0
sequence analysis
-
expression in Escherichia coli
-
transformed SK32 cells stably expressing one of the wild type Pex5p isoforms, Pex5pM and S restore the processing of Aox, but Pex5pL does not
-
sequence analysis
Cucurbita sp.
-
gene aoxA, seuence comparisons, recombinant expression from plasmid in Aspergillus nidulans strain MH11036, complementation of enzyme deficient aoxADELTA strain MH11074, expression as GFP-tagged enzyme showing PexE-dependent peroxisomal localisation
-
expression in Escherichia coli of 2 genes: ACX1.1 and ACX1.2, sequence comparison with other species
-
expressed in Escherichia coli strains BL21 and C41, and in COS-7 cells (His-tagged enzyme)
-
expression as His-tagged protein in Spodoptera frugiperda cells via infection with Baculovirus
-
expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the null phenotype, overview
-
SCOX expression analysis in peroxisomal acyl-coenzyme A oxidase deficiency patients, overview
-
overexpression in Escherichia coli
-
sequence analysis, expression analysis during development
-
expression in COS-7 cells
-, Q8HYL8
ACO-I and ACO-II; expression in Escherichia coli
-
cloned into a bacterial expression vector pLM1 with six continous His codons attached to the 5' end of the gene, overexpression of wild-type ands mutant enzymes E421D, E421A, E421Q and E421G in Escherichia coli
-
expressed in Escherichia coli
P07872
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
His-tagged
-
into vector pTZ18R
-
sequence analysis and regulation
-
expression in Escherichia coli as an active, N-terminal tagged His6 fusion protein
O74935, -
expression of His-tagged enzyme in Escherichia coli
-
genes POX1-POX6, heterologous co-expression of the different isozymes with polyhydroxyalkanoate synthase (phaC) of Pseudomonas aeruginosa in Yarrowia lipolytica strains, subcloning in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C159T
-, Q33DR0
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
C159T/C420S
-, Q33DR0
activity less than one tenth of that of the wild type
C159T/C420S/C424V
-, Q33DR0
shows no activity at all
C159T/C424V
-, Q33DR0
activity less than one tenth of that of the wild type
C420S
-, Q33DR0
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
C420S/424V
-, Q33DR0
activity less than one tenth of that of the wild type
C424V
-, Q33DR0
98% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; looses more than half of the activity after incubation with N-Ethylmaleimide
C159T
Arthrobacter ureafaciens NBRC 12140
-
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
-
C420S
Arthrobacter ureafaciens NBRC 12140
-
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
-
C424V
Arthrobacter ureafaciens NBRC 12140
-
looses more than half of the activity after incubation with N-Ethylmaleimide
-
G432R
-
conversion of Aox from component A to components B and C is completely prevented at both 30C and 37C
G231V
Q15067
the mutation in combination with skipping of exon 13 leads to peroxisomal acyl-CoA oxidase deficiency
E421A
-
inactive mutant enzyme
E421A
-
does not show any isomerase activity
E421D
-
Km-value for octanoyl-CoA is 1.23fold higher than the wild-type value. The turnover number for octanoyl-CoA is 1.6fold lower than activity of the wild-type enzyme
E421D
-
isomerase activity is decreased for all tested cis- and trans-substrates compared with that of wild-type enzyme
E421G
-
inactive mutant enzyme
E421Q
-
inactive mutant enzyme
T138I
-
compromised in wound-response signaling owing to a deficiency in jasmonic acid synthesis, FAD is not bound in the mutant protein
additional information
-
mutants defective in ACX1, ACX3, or ACX4 have reduced fatty acyl-CoA oxidase activity, acx1 acx2 double mutants display enhanced indole-3-butyric acid resistance and are sucrose dependent during seedling development, acx1 acx3 and acx1 acx5 double mutants display enhanced indole-3-butyric acid resistance but remain sucrose independent
additional information
O65201, Q9LLH9
acx1-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is unaltered in the acx1-1 mutant, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx1-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype, wound-induced increase in jasmonic acid is only compromised in the acx1-1 mutant; acx2-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx2-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype
additional information
-
the ibr3-1 acx3-4 double mutant shows greatly enhanced indole-3-butyric acid resistance
additional information
-
generation of higher-order acx mutants, the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type
additional information
Arabidopsis thaliana Col-0
-
generation of higher-order acx mutants, the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type
-
R210H
-
naturally occuring apparent homozygous missense mutation c.629G/A of SCOX in a peroxisomal acyl-coenzyme A oxidase deficiency patient
additional information
-
ACOX1-/- mice show twofold increased expression of isozyme ACOX1a compared to wild-type mice, ACOX1b-/- and ACOX1a-/- phenotypes, overview. Expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the hepatic null phenotype, but with only weak reversal of the hepatic steatosis phenotype in the mice, overview. Expression of human isozyme ACOX1a has only poor effects
E421Q
-
does not show any isomerase activity
additional information
-
OAF1-gene disrupted construct with reduced number of peroxisomes, no longer inducible by oleate
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-, Q33DR0
useful for the determination of free fatty acids
analysis
Arthrobacter ureafaciens NBRC 12140
-
useful for the determination of free fatty acids
-
degradation
-
ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
degradation
Beauveria bassiana GHA
-
ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
-
biotechnology
-
potential depolluting agent by degradation of oils; several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids
analysis
-
amperometric propionate sensor
additional information
-
solvent-accessible acyl binding pocket is not required for oxygen reactivity, the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity
additional information
-
inability of ACX1, ACX3, and ACX4 to fully compensate for one another in indole-3-butyric acid-mediated root elongation inhibition and ability of ACX2 and ACX5 to contribute to indole-3-butyric acid response suggests that indole-3-butyric acid-response defects in acx mutants may reflect indirect blocks in peroxisomal metabolism and indole-3-butyric acid beta-oxidation, rather than direct enzymatic activity of ACX isozymes on indole-3-butyric acid-CoA
nutrition
-
engineering of plants with increased content of monocarboxylic fatty acids in this essential oil crop by enzyme overexpression
additional information
-
novel Pex5pM is functional and a seven amino acids-insertion, which is present in the L isoform but absent in the M isoform, plays some role in the process of maturation of Aox
additional information
-, Q4QRE2
ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity; ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity
medicine
-
ACOX1 is a rate-limiting enzyme in peroxisomal fatty acids beta-oxidation and its deficiency is associated with a lethal, autosomal recessive disease, called pseudoneonatal-adrenoleukodystrophy
additional information
-, Q5VRH3, Q69XR7
three distinct ACX genes, ACX1 is upregulated by wounding, both locally and systemically, ACX1 may play a role in the synthesis of jasmonic acid in response to wounding; three distinct ACX genes, expression of ACX2 remains unchanged by wounding, ACX2 may be involved in providing germinating seeds with sugar and energy; three distinct ACX genes, expression of ACX3 remains unchanged by wounding
medicine
-
AOX activity is negatively correlated with postprandial triacylglycerol levels
additional information
-
isomerase activity of rat peroxisomal acyl-CoA oxidase I, is probably due to a spontaneous process driven by thermodynamic equilibrium with formation of a conjugated structure after deprotonation of substrate alpha-proton
additional information
-
nervonic acid is discharged from the spore into the external medium during firing along with the catalase and ACOX enzymes